1L5T
Crystal Structure of a Domain-Opened Mutant (R121D) of the Human Lactoferrin N-lobe Refined From a Merohedrally-Twinned Crystal Form.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | ROTATING ANODE |
| Source details | RIGAKU RU200 |
| Temperature [K] | 295 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-03-01 |
| Detector | RIGAKU RAXIS IIC |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 31 |
| Unit cell lengths | 151.300, 151.300, 48.600 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 * - 3.000 |
| Rwork | 0.139 |
| R-free | 0.19900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lct |
| RMSD bond length | 0.005 |
| RMSD bond angle | 0.017 |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((AGROVATA) |
| Phasing software | X-PLOR |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 * | 3.110 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.115 | 0.418 |
| Number of reflections | 23882 * | |
| <I/σ(I)> | 6.1 | 1.8 |
| Completeness [%] | 96.0 | 93 |
| Redundancy | 2.8 | 2.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | MICRODIALYSIS | 8 | 298 | concentrated solution of the protein (50-80 mg mL-1), 0.01 M Tris-HCl, pH 8.0, 12% (v/v) isopropanol, MICRODIALYSIS, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | Tris-HCl | 0.05 (M) | pH8.0 |
| 2 | 1 | drop | 0.1 (M) | ||
| 3 | 1 | drop | ferric nitrilotriacetate | 0.01 (M) | |
| 4 | 1 | drop | protein | 50-80 (mg/ml) | |
| 5 | 1 | reservoir | Tris-HCl | 0.01 (M) | pH8.0 |
| 6 | 1 | reservoir | 2-propanol | 12 (%(v/v)) |
